Unmasking the ancestral activity of integron integrases reveals a smooth evolutionary transition during functional innovation - Archive ouverte HAL Access content directly
Journal Articles Nature Communications Year : 2016

Unmasking the ancestral activity of integron integrases reveals a smooth evolutionary transition during functional innovation

(1) , (1) , (2) , (1) , (3) , (1)
1
2
3

Abstract

Tyrosine (Y)-recombinases have evolved to deliver mechanistically different reactions on a variety of substrates, but these evolutionary transitions are poorly understood. Among them, integron integrases are hybrid systems recombining single-and double-stranded DNA partners. These reactions are asymmetric and need a replicative resolution pathway, an exception to the canonical second strand exchange model of Y-recombinases. Integron integrases possess a specific domain for this specialized pathway. Here we show that despite this, integrases are still capable of efficiently operating the ancestral second strand exchange in symmetrical reactions between double-stranded substrates. During these reactions, both strands are reactive and Holliday junction resolution can follow either pathway. A novel deep-sequencing approach allows mapping of the crossover point for the second strand exchange. The persistence of the ancestral activity in integrases illustrates their robustness and shows that innovation towards new recombination substrates and resolution pathways was a smooth evolutionary process.
Fichier principal
Vignette du fichier
ncomms10937.pdf (1.24 Mo) Télécharger le fichier
Origin : Publisher files allowed on an open archive
Loading...

Dates and versions

pasteur-01292328 , version 1 (22-03-2016)

Licence

Attribution - CC BY 4.0

Identifiers

Cite

Jose Antonio Escudero, Celine Loot, Vincent Parissi, Aleksandra Nivina, Christiane Bouchier, et al.. Unmasking the ancestral activity of integron integrases reveals a smooth evolutionary transition during functional innovation. Nature Communications, 2016, 7, pp.Article number 10937. ⟨10.1038/ncomms10937⟩. ⟨pasteur-01292328⟩

Collections

PASTEUR CNRS ANR
173 View
167 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More